3V11

Structure of the ternary initiation complex AIF2:GDPNP:methionylated initiator TRNA

Summary for 3V11

• Entry DOI: 10.2210/pdb3v11/pdb
• Related: 2AHO 2QMU 3CW5
• Descriptor: Translation initiation factor 2 subunit gamma, Translation initiation factor 2 subunit alpha, Translation initiation factor 2 subunit beta, ... (7 entities in total)
• Functional Keywords: gtp binding module, initiator trna carrier, gtp and trna, translation-rna complex, translation/rna
• Biological source: Sulfolobus solfataricus; More
• Total number of polymer chains: 4
• Total formula weight: 117490.56

Authors

Mechulam, Y.,Schmitt, E. (deposition date: 2011-12-09, release date: 2012-03-28, Last modification date: 2023-09-13)

Primary citation

Schmitt, E.,Panvert, M.,Lazennec-Schurdevin, C.,Coureux, P.D.,Perez, J.,Thompson, A.,Mechulam, Y.
Structure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNA.
Nat.Struct.Mol.Biol., 19:450-454, 2012

PubMed Abstract: Eukaryotic and archaeal translation initiation factor 2 (e/aIF2) is a heterotrimeric GTPase that has a crucial role in the selection of the correct start codon on messenger RNA. We report the 5-Å resolution crystal structure of the ternary complex formed by archaeal aIF2 from Sulfolobus solfataricus, the GTP analog GDPNP and methionylated initiator tRNA. The 3D model is further supported by solution studies using small-angle X-ray scattering. The tRNA is bound by the α and γ subunits of aIF2. Contacts involve the elbow of the tRNA and the minor groove of the acceptor stem, but not the T-stem minor groove. We conclude that despite considerable structural homology between the core γ subunit of aIF2 and the elongation factor EF1A, these two G proteins of the translation apparatus use very different tRNA-binding strategies.

PubMed: 22447243
DOI: 10.1038/nsmb.2259

Experimental method

X-RAY DIFFRACTION (5 Å)